Open AccessCrystallization and preliminary X‐ray diffraction analysis of a complex between the electron‐transfer partners hexameric Cu‐containing nitrite reductase and pseudoazurin
Author(s) -
Hira Daisuke,
Nojiri Masaki,
Suzuki Shinnichiro
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108040219
Subject(s) - crystallography , tetragonal crystal system , chemistry , nitrite reductase , polyethylene glycol , crystallization , electron transfer , protein crystallization , diffraction , resolution (logic) , crystal structure , nitrite , photochemistry , organic chemistry , optics , physics , artificial intelligence , computer science , nitrate
The complex between Cu‐containing nitrite reductase (HdNIR) and its electron‐donor protein pseudoazurin (HdPAz) from Hyphomicrobium denitrificans has been crystallized. The crystals were obtained from a mixture of the two proteins using the hanging‐drop vapour‐diffusion method in the presence of polyethylene glycol (PEG) and 2‐methyl‐2,4‐pentanediol (MPD) as precipitants. SDS–PAGE analysis demonstrated that the crystals contained both proteins. The X‐ray diffraction experiment was carried out at SPring‐8 and diffraction data were collected to 3.3 Å resolution. The crystals were tetragonal (space group P 4 1 2 1 2), with unit‐cell parameters a = b = 130.39, c = 505.55 Å. Preliminary analysis indicated that there was one HdNIR and at least two HdPAz molecules in the asymmetric unit of the crystal.